The DOI matches its Crossref record; 155 of the 158 references it cites were found in a registry or an index.
Missing Pieces in the NF-κB Puzzle
Open accessAbstract
The regulation of the transcription factor NF-kappaB activity occurs at several levels including controlled cytoplasmic-nuclear shuttling and modulation of its transcriptional activity. A critical component in NF-kappaB regulation is the IkappaB kinase (IKK) complex. This review is focused on recent progress as well as unanswered questions regarding the regulation and function of NF-kappaB and IKK.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In the NF-κB system (e.g. [2020-2024]) (Fig 8), NF-κB is normally held inactive in the cytoplasm by binding to an inhibitor IκB (often IκBα). Pro-inflammatory cytokines such as TNF-α, LPS [2025-2030] and IL-1 [2031] act by binding to receptors at the cell surface and initiating signalling pathways that lead to the activation of a particular kinase, IκB kinase or IKK. This kinase phosphorylates the”
From Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases (2009) · cites this paper as [2020]
Citations
Cites
1 retracted
RETRACTED: DNA-PKcs Is Required for Activation of Innate Immunity by Immunostimulatory DNA
Chu, W., Gong, X., Li, Z.-W., Takabayashi, K., Ouyang, H., Chen, Y., Lois, A. F., Chen, D. J., Li, G. C., Karin, M., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00194-x · Cited by 178
Self-citationRetractedA Toll-like receptor recognizes bacterial DNA
Hemmi, H., Takeuchi, O., Kawai, T., Kaisho, T., Sato, S., Sanjo, H., Matsumoto, M., Hoshino, K., Wagner, H., Takeda, K., et al. (2000) · Nature · doi:10.1038/35047123 · Cited by 6,491
Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
Alexopoulou, L., Holt, A. C., Medzhitov, R., & Flavell, R. A. (2001) · Nature · doi:10.1038/35099560 · Cited by 6,129
NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune Responses
Ghosh, S., May, M. J., & Kopp, E. B. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.225 · Cited by 5,182
Self-citationPhosphorylation meets ubiquitination: the control of NF-κB activity
Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766
Self-citationNF-κB at the crossroads of life and death
Karin, M., & Lin, A. (2002) · Nature Immunology · doi:10.1038/ni0302-221 · Cited by 2,709
Self-citationTAK1 is a ubiquitin-dependent kinase of MKK and IKK
Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125
A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
DiDonato, J. A., Hayakawa, M., Rothwarf, D. M., Zandi, E., & Karin, M. (1997) · Nature · doi:10.1038/41493 · Cited by 2,125
Self-citationIKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation
Mercurio, F., Zhu, H., Murray, B. W., Shevchenko, A., Bennett, B. L., Li, J. W., Young, D. B., Barbosa, M. S., Mann, M., Manning, A. M., et al. (1997) · Science · doi:10.1126/science.278.5339.860 · Cited by 2,042
Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872
Cited by
Sorted by citations
Items 601–700 of 1,025
Expression of the Bcl-3 proto-oncogene suppresses p53 activationPreprint
Kashatus, D. F., Cogswell, P., & Baldwin, A. S. (2005) · Genes & Development · doi:10.1101/gad.1352206 · Cited by 137
“Based on the ability of NF- B to regulate cell death pathways (Ghosh and Karin 2002; Kucharczak et al. 2003) and on recent studies that suggest a link between Bcl-3 and the DNA damage response (Boulton et al. 2002; Watanabe et al. 2003), we have investigated a potential role for Bcl-3 in regulating…”
BackgroundJia, L., Liu, J., Song, Z., Pan, X., Chen, L., Cui, X. K., & Wang, Μ. (2012) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.2012.01529.x · Cited by 137
“The translocation of NF-kB to the cell nucleus is preceded by the phosphorylation, ubiquitination and proteolytic degradation of IkBa.([29]) To determine whether inhibition of Ab-induced NF-kB activation by berberine was due to regulation of IkBa degradation, we examined IkBa phosphorylation by Western blot analysis u…”
InfluentialmiR-218 inhibits the invasive ability of glioma cells by direct downregulation of IKK-β
Song, L., Huang, Q., Chen, K., Liu, L., Lin, C., Dai, T., Yu, C., Wu, Z., & Li, J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.10.003 · Cited by 138
“Nuclear factor-kappa B (NF-jB) is a transcription factor with pleiotropic activity owing to the central roles it plays in various biological processes [1,2].”
Krishnan, A. V., & Feldman, D. (2009) · Endocrine Related Cancer · doi:10.1677/erc-09-0139 · Cited by 139
“Free NFkB then translocates to the nucleus and activates the transcription of pro-inflammatory cytokines, chemokines, and anti-apoptotic factors (Ghosh & Karin 2002).”
BackgroundLipocalin 2 Deficiency Dysregulates Iron Homeostasis and Exacerbates Endotoxin-Induced Sepsis
Srinivasan, G., Aitken, J. D., Zhang, B., Carvalho, F. A., Chassaing, B., Shashidharamurthy, R., Borregaard, N., Jones, D. P., Gewirtz, A. T., & Vijay–Kumar, M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200892 · Cited by 143
Haydar, D., Cory, T. J., Birket, S. E., Murphy, B. S., Pennypacker, K. R., Sinai, A. P., & Feola, D. J. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1801228 · Cited by 136
“Additionally, IKKb activation requires phosphorylation of two serines; thus, regulation of IKKb activation involves tight control of its trans-autophosphorylation as well as its phosphorylation by the upstream kinases (18, 20, 21).”
Sadikot, R. T., Zeng, H., Joo, M., Everhart, M. B., Sherrill, T. P., Li, B., Cheng, D., Yull, F. E., Christman, J. W., & Blackwell, T. S. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.8.4923 · Cited by 136
Li, Z., Nickkholgh, A., Yi, X., Bruns, H., Groß, M.-L., Hoffmann, K., Mohr, E., Zorn, M., Büchler, M. W., & Schemmer, P. (2009) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2009.00672.x · Cited by 136
Zampetaki, A., Zhang, Z., Hu, Y., & Xu, Q. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00919.2004 · Cited by 136
“and the released NF-κB translocates to the nucleus, binds to DNA and activates gene transcription (9).”
Moon, D., Kim, M.-O., Kang, S.-H., Choi, Y. H., & Kim, G. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.09.013 · Cited by 137
Notch3 and pre‐TCR interaction unveils distinct NF‐κB pathways in T‐cell development and leukemia
Vacca, A., Felli, M. P., Palermo, R., Mario, G. D., Calce, A., Giovine, M. D., Frati, L., Gulino, A., & Screpanti, I. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600996 · Cited by 135
“geneous collection of homodimers and heterodimers (Ghosh and Karin, 2002).”
Mechanisms of glucocorticoid-induced apoptosis in hematologic malignancies: updates
Frankfurt, O., & Rosen, S. T. (2004) · Current Opinion in Oncology · doi:10.1097/01.cco.0000142072.22226.09 · Cited by 134
Sanchez, J. F., Sniderhan, L. F., Williamson, A. L., Fan, S., Chakraborty‐Sett, S., & Maggirwar, S. B. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.13.4649-4662.2003 · Cited by 134
Gomez, P., Pillinger, M. H., Attur, M. G., Marjanović, N., Dave, M., Park, J., Bingham, C. O., Al-Mussawir, H., & Abramson, S. B. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.10.6924 · Cited by 134
Deactivation of the kinase IKK by CUEDC2 through recruitment of the phosphatase PP1
Li, H., Liu, H., Wang, C., Zhang, J.-Y., Man, J.-H., Gao, Y.-F., Zhang, P., Li, W., Zhao, J., Pan, X., et al. (2008) · Nature Immunology · doi:10.1038/ni.1600 · Cited by 134
“org/molecule/query?afcsid=A001172 ">A001172 ), and a regulatory subunit, NF-κB essential modulator (NEMO; also called IKKγ”
BackgroundAhn, K. S., Sethi, G., Jain, A. K., Jaiswal, A. K., & Aggarwal, B. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601162200 · Cited by 134
Arora, S., Bhardwaj, A., Srivastava, S. K., Singh, S., McClellan, S. B., Wang, B., & Singh, A. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021573 · Cited by 134
Cheong, R., Bergmann, A., Werner, S. L., Regal, J. A., Hoffmann, A., & Levchenko, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510085200 · Cited by 131
da Silva, K. A. B. S., Paszcuk, A. F., Passos, G. F., da Silva, E. S., Bento, A. F., Meotti, F. C., & Calixto, J. Β. (2011) · Pain · doi:10.1016/j.pain.2011.04.005 · Cited by 135
Pang, R. W. C., Lee, T. K., Poon, R. T. P., Fan, S. T., Wong, K., Kwong, Y., & Tse, E. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.12.030 · Cited by 134
Toll-like receptors, wound healing, and carcinogenesis
Kluwe, J., Mencin, A. M., & Schwabe, R. F. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0426-z · Cited by 137
“NF-κB regulates the transcription of several hundred genes with κB sites, among them a number of antiapoptotic genes such as Bcl-2, iNOS, c-Flip, IAPs, and Traf molecules [85].”
NF-κB signaling in skeletal muscle: prospects for intervention in muscle diseases
Mourkioti, F., & Rosenthal, N. A. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0308-4 · Cited by 134
Nuclear Factor-κB Activation as a Pathological Mechanism of Lipid Metabolism and Atherosclerosis
Yu, X., Zheng, X., & Tang, C. (2015) · Advances in clinical chemistry · doi:10.1016/bs.acc.2015.03.004 · Cited by 132
Zhang, Y., Ting, A. T., Marcu, K. B., & Bliska, J. B. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.12.7939 · Cited by 133
Schwab, M., Reynders, V., Loitsch, S. M., Steinhilber, D., Stein, J. M., & Schröder, O. (2007) · Molecular Immunology · doi:10.1016/j.molimm.2007.04.010 · Cited by 133
Romieu, R., Landesman‐Bollag, E., Seldin, D. C., & Sonenshein, G. E. (2002) · PubMed · Cited by 133
Carrero, I., Gonzalo, M. R., Martin, B., Sanz-Anquela, J. M., Arévalo-Serrano, J., & Gonzalo-Ruiz, A. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.05.004 · Cited by 132
Medeiros, R., Otuki, M. F., Avellar, M. C. W., & Calixto, J. Β. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.12.005 · Cited by 132
DEAD-box helicase DP103 defines metastatic potential of human breast cancers
Shin, E. M., Hay, H. S., Lee, M. H., Goh, J. N., Tan, T. Z., Sen, Y. P., Lim, S. W., Yousef, E. M., Ong, H. T., Thike, A. A., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci73451 · Cited by 132
Curcumin and Inflammatory Bowel Disease: Potential and Limits of Innovative Treatments
Brumatti, L. V., Marcuzzi, A., Tricarico, P. M., Zanin, V., Girardelli, M., & Bianco, A. M. (2014) · Molecules · doi:10.3390/molecules191221127 · Cited by 134
New insights into the resolution of inflammation
Gilroy, D. W., & Maeyer, R. P. H. D. (2015) · Seminars in Immunology · doi:10.1016/j.smim.2015.05.003 · Cited by 134
Ionizing radiation-induced NF-κB activation requires PARP-1 function to confer radioresistance
Veuger, S. J., Hunter, J. E., & Durkacz, B. W. (2008) · Oncogene · doi:10.1038/onc.2008.439 · Cited by 134
“Upon stimulation by inflammatory cytokines or DNA damage, several signalling cascades converge at the IKK complex which phosphorylates and targets IκBα for degradation, promoting nuclear translocation of NF-κB, where it binds to enhancer/promoter regions of target genes, activating transcription (Ghosh and Karin, 2002…”
RetractedInflammation-activated Protein Kinases as Targets for Drug Development
Karin, M. (2005) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200504-034sr · Cited by 132
Self-citationLymphotoxin and lipopolysaccharide induce NF‐κB‐p52 generation by a co‐translational mechanism
Mordmüller, B. G., Krappmann, D., Esen, M., Wegener, E., & Scheidereit, C. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor710 · Cited by 132
A Structural Guide to Proteins of the NF- B Signaling ModulePreprint
Huxford, T., & Ghosh, G. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000075 · Cited by 135
The atypical PKCs in inflammation: NF‐κB and beyond
Díaz-Meco, M. T., & Moscat, J. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01093.x · Cited by 132
Fradet, V., Lessard, L., Bégin, L. R., Karakiewicz, P. I., Mes‐Masson, A., & Fred Saad, C. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-0764 · Cited by 131
Tong, W., Wang, Q., Sun, D., & Suo, J. (2016) · Oncology Letters · doi:10.3892/ol.2016.5148 · Cited by 131
“NF-κ B activation proceeds sequentially through the activation of IKK, phosphorylation of IkB α , degradation of IkB α, release of NF-κ B, p65 phosphorylation and p65 nuclear translocation (47).”
Anti-apoptotic signalling by the Dot/Icm secretion system ofL. pneumophila
Abu-Zant, A., Jones, S. C., Asare, R., Suttles, J., Price, C. T. D., Graham, J. E., & Kwaik, Y. A. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00785.x · Cited by 145
“During late stages of intracellular replication, the LCP membrane becomes disrupted and the bacteria escape into the cytoplasm where they continue their terminal rounds of proliferation (Molmeret and Abu Kwaik, 2002; Molmeret et al., 2004a,b).”
Tegethoff, S., Behlke, J., & Scheidereit, C. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.6.2029-2041.2003 · Cited by 132
“IKK is essential for activation of IKK and IKK by all physiological stimuli analyzed, and C-terminal sequences of IKK are specifically required for responsiveness of the complex to proinflammatory stimuli ( 10 , 31, 39).”
BackgroundIκB Kinase Is an Essential Component of the Tpl2 Signaling Pathway
Waterfield, M. R., Jin, W., Reiley, W. W., Zhang, M., & Sun, S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.6040-6048.2004 · Cited by 134
“Recombinant IKK (10 ng) and IKK (5 ng) were incubated for 15 min (at 25°C) with either the solvent DMSO () or the IKK inhibitor PS1145 (10 M), and their catalytic activity was analyzed by using GST-IB ( 1-54 ) as a substrate.”
BackgroundMethodInfluentialStructure of a NEMO/IKK-Associating Domain Reveals Architecture of the Interaction Site
Rushe, M. M., Silvian, L. F., Bixler, S. A., Chen, L. L., Cheung, A. E., Bowes, S., Cuervo, H., Berkowitz, S. A., Zheng, T. S., Guckian, K. M., et al. (2008) · Structure · doi:10.1016/j.str.2008.02.012 · Cited by 133
Gupta, M., Gupta, S. K., Hoffman‐Liebermann, B., & Liebermann, D. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600950200 · Cited by 131
Crossroads of Estrogen Receptor and NF-κB Signaling
Biswas, D. K., Singh, S., Shi, Q., Pardee, A. B., & Iglehart, J. D. (2005) · Science s STKE · doi:10.1126/stke.2882005pe27 · Cited by 130
Many faces of NF-κB signaling induced by genotoxic stress
Wu, Z., & Miyamoto, S. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0227-9 · Cited by 131
Viemann, D., Goebeler, M., Schmid, S., Klimmek, K., Sorg, C., Ludwig, S., & Roth, J. (2004) · Blood · doi:10.1182/blood-2003-09-3296 · Cited by 132
Shibata, W., Maeda, S., Hikiba, Y., Yanai, A., Ohmae, T., Sakamoto, K., Nakagawa, H., Ogura, K., & Omata, M. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.5.2681 · Cited by 130
Links between Innate Immunity and Normal Tissue Radiobiology
Schaue, D., & McBride, W. H. (2010) · Radiation Research · doi:10.1667/rr1931.1 · Cited by 134
“Related cytoprotective proteins that are up-regulated include members of the Bcl-2 and inhibitor of apoptosis (IAP) families (105).”
The role of monocytes in atherosclerotic coronary artery disease
Pamukçu, B., Lip, G. Y. H., Devitt, A., Griffiths, H. R., & Shantsila, E. (2010) · Annals of Medicine · doi:10.3109/07853890.2010.497767 · Cited by 127
“Nuclear factor κ B (NF κ B) and mitogen-activated protein kinase pathways appear to be major participants is such processes (31).”
Induction of Notch signaling by tumor necrosis factor in rheumatoid synovial fibroblasts
Ando, K., Kanazawa, S., Tetsuka, T., Ohta, S., Jiang, X., Tada, T., Kobayashi, M., Matsui, N., & Okamoto, T. (2003) · Oncogene · doi:10.1038/sj.onc.1206965 · Cited by 129
Yamazaki, S., Muta, T., Matsuo, S., & Takeshige, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409983200 · Cited by 129
Kong, X., Yan, H., Chen, L., Dong, L., Yang, W., Liu, Q., Yu, L., Huang, D., Liu, S., Liu, H., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20062611 · Cited by 134
Comparative Analysis of Apoptosis and Inflammation Genes of Mice and HumansPreprint
Reed, J. C., Doctor, K. S., Rojas, A. M., Zapata, J. M., Stehlik, C., Fiorentino, L., Damiano, J. S., Roth, W., Matsuzawa, S.-I., Newman, R. M., et al. (2003) · Genome Research · doi:10.1101/gr.1053803 · Cited by 129
“Of those, I BK , I BK , and I BK form a protein complex in which I BK and I BK represent the catalytic subunits, whereas I BK is a regulatory subunit (lacking a kinase domain) and is not structurally related to the and subunits (Karin and Ben-Neriah 2000; Ghosh and Karin 2002).”
BackgroundNikolaou, K., Tsagaratou, A., Eftychi, C., Kollias, G. A., Mosialos, G., & Talianidis, I. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.04.026 · Cited by 129
Yan, M., Xu, Q., Zhang, P., Zhou, X., Zhang, Z., & Chen, W. (2010) · BMC Cancer · doi:10.1186/1471-2407-10-437 · Cited by 128
“NF- B can then enter the nucleus to regulate the expression of genes involved in cell proliferation, cell survival and apoptosis [8,9].”
Genome reading by the NF-κB transcription factors
Mulero, M. C., Wang, V. Y., Huxford, T., & Ghosh, G. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz739 · Cited by 130
Reiniers, M. J., van Golen, R. F., van Gulik, T. M., & Heger, M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5486 · Cited by 134
NF‐κB activation by protein kinase C isoforms and B‐cell function
Moscat, J., Díaz-Meco, M. T., & Rennert, P. D. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor704 · Cited by 128
“The physiological roles of each of these subunits have been revealed by studies of various KO mice (Ghosh & Karin, 2002).”
BackgroundThe Role and Regulation of the Nuclear Factor Kappa B Signalling Pathway in Human Labour
Lappas, M., & Rice, G. E. (2006) · Placenta · doi:10.1016/j.placenta.2006.05.011 · Cited by 127
Harikumar, K. B., Sung, B., Tharakan, S. T., Pandey, M. K., Joy, B., Guha, S., Krishnan, S., & Aggarwal, B. B. (2010) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0565 · Cited by 128
Piette, J. G., Volanti, C., Vantieghem, A., Matroule, J., Habraken, Y., & Agostinis, P. (2003) · Biochemical Pharmacology · doi:10.1016/s0006-2952(03)00539-2 · Cited by 127
Early Alterations in Neutrophil Activation Are Associated with Outcome in Acute Lung Injury
Yang, K., Arcaroli, J. J., & Abraham, E. H. (2003) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200207-664oc · Cited by 127
“Because complex to move to the nucleus, where it can bind to specific neutrophils appear to play a major role in the development of promoter sequences, associate with coactivators, and initiate ALI, we examined the relationships between clinical outcome and transcription ( 11 , 12).”
BackgroundVega, M. I., Jazirehi, A. R., Huerta‐Yépez, S., & Bonavida, B. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.4.2174 · Cited by 129
AIP1/DAB2IP, a Novel Member of the Ras-GAP Family, Transduces TRAF2-induced ASK1-JNK Activation
Zhang, H., Zhang, R., Luo, Y., D’Alessio, A., Pober, J. S., & Wang, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407617200 · Cited by 125
Involvement of PKCα/β in TLR4 and TLR2 dependent activation of NF-κB
Asehnoune, K., Strassheim, D., Mitra, S., Kim, J. Y., & Abraham, E. H. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.08.005 · Cited by 127
Recruitment of IκBα to the hes1 promoter is associated with transcriptional repression
Aguilera, C. N., Hoya-Arias, R., Haegeman, G., Espinosa, L., & Bigas, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404429101 · Cited by 126
IKKα Is Required to Maintain Skin Homeostasis and Prevent Skin Cancer
Liu, B., Xia, X., Zhu, F., Park, E., Carbajal, S., Kiguchi, K., DiGiovanni, J., Fischer, S. M., & Hu, Y. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.07.017 · Cited by 124
Bosco, M. C., Pierobon, D., Blengio, F., Raggi, F., Vanni, C., Gattorno, M., Eva, A., Novelli, F., Cappello, P., Giovarelli, M., et al. (2010) · Blood · doi:10.1182/blood-2010-06-292136 · Cited by 125
Zhou, Y., Eppenberger‐Castori, S., Marx, C., Yau, C. S. F., Scott, G. K., Eppenberger, U., & Benz, C. C. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.09.006 · Cited by 127
Lebron, F., Vassallo, R., Puri, V., & LIMPER, A. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301426200 · Cited by 125
Welsh, N., Cnop, M., Kharroubi, I., Bugliani, M., Lupi, R., Marchetti, P., & Eizirik, D. L. (2005) · Diabetes · doi:10.2337/diabetes.54.11.3238 · Cited by 125
Wan, M.-L., Wang, Y., Zeng, Z. R., Deng, B., Zhu, B., Cao, T., Li, Y., Xiao, J., Han, Q., & Wu, Q. (2020) · Bioscience Reports · doi:10.1042/bsr20200265 · Cited by 128
Hatziieremia, S., Gray, A. I., Ferro, V. A., Paul, A., & Plevin, R. J. (2006) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706856 · Cited by 124
“We found that cardamonin has little effect on IkBa degradation, suggesting that the effect of this chalcone is unlikely to be at the level of IKKb activation and subsequent phosphorylation, ubiquination and degradation of IkBa (Ghosh and Karin, 2002).”
BackgroundInducible Phosphorylation of NF-κB p65 at Serine 468 by T Cell Costimulation Is Mediated by IKKϵ
Mattioli, I., Geng, H. Z., Sebald, A., Hodel, M., Bucher, C., Kracht, M., & Schmitz, M. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508045200 · Cited by 126
NF-κB RelA opposes epidermal proliferation driven by TNFR1 and JNKPreprint
Zhang, J. Y., Green, C. L., Tao, S., & Khavari, P. A. (2004) · Genes & Development · doi:10.1101/gad.1160904 · Cited by 122
Constitutive IKK2 activation in acinar cells is sufficient to induce pancreatitis in vivo
Baumann, B., Wagner, M., Aleksic, T., von Wichert, G., Weber, C. K., Adler, G., & Wirth, T. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30876 · Cited by 123
“Consequently, NF-κB dimers are released from their inactive cytosolic state, enter the nucleus, and induce transcription of target genes (4).”
BackgroundSethi, G., Ahn, K. S., Sung, B., & Aggarwal, B. B. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-2424 · Cited by 124
“Pinitol InhibitsTNF-Dependent IKBADegradation Because InBa degradation is required for activation of NF-nB (29), we investigated whether inhibition of TNFinduced NF-nB activation by pinitol was due to inhibition of InBa degradation.”
Role of NF-κB in thyroid cancer
Pacifico, F., & Leonardi, A. (2009) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.10.010 · Cited by 124
Linkage between EGFR family receptors and nuclear factor kappaB (NF‐κB) signaling in breast cancer
Biswas, D. K., & Iglehart, J. D. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20785 · Cited by 123
“The NF-kB family consists of at least five members, including three rel (mammalian reticuloendotheliosis) proteins (rel A/p65, rel B and c-rel) and their processed partners, p100/p52 and p105/p50 (Ghosh and Karin, 2002, Karin and Lin, 2002, Nakshatri and Goulet, 2002; Karin and Lin, 2002).”
BackgroundZhang, H., Moochhala, S., & Bhatia, M. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.6.4320 · Cited by 122
Niu, J., Chang, Z., Peng, B., Xia, Q., Lu, W., Huang, P., Tsao, M., & Chiao, P. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m606878200 · Cited by 121
Expression of Nuclear Factor-κB and IκBα Proteins in Prostatic Adenocarcinomas
Ross, J. S., Kallakury, B., Sheehan, C. E., Fisher, H. A. �., Kaufman, R. P., Kaur, P., Gray, K., & Stringer, B. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-0543-3 · Cited by 121
Manna, S. K., Aggarwal, R. S., Sethi, G., Aggarwal, B. B., & Ramesh, G. T. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2394 · Cited by 124
Modulation of Nod2-dependent NF-κB signaling by the actin cytoskeleton
Legrand-Poels, S., Kustermans, G., Bex, F., Kremmer, E., Kufer, T. A., & Piette, J. G. (2007) · Journal of Cell Science · doi:10.1242/jcs.03424 · Cited by 123
“Upon stimulation with proinflammatory agents such as cytokines (TNF , IL-1 ) or bacterial lipopolysaccharides (LPS), I B is phosphorylated, polyubiquitinated, then degraded by the 26S proteasome, allowing NF- B to translocate to the nucleus and transactivate its target genes (for reviews, see Karin and Ben-Neriah, 200…”
Sato, S. (2006) · International Immunology · doi:10.1093/intimm/dxl082 · Cited by 123
PKCζ at the crossroad of NF-κB and Jak1/Stat6 signaling pathways
Moscat, J., Rennert, P. D., & Díaz-Meco, M. T. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401823 · Cited by 121
Transducing signals from antigen receptors to nuclear factor κB
Ruland, J., & Mak, T. W. (2003) · Immunological Reviews · doi:10.1034/j.1600-065x.2003.00049.x · Cited by 121
X-ray Crystal Structure of an IκBβ·NF-κB p65 Homodimer Complex
Malek, S., Huang, D.-B., Huxford, T., Ghosh, S., & Ghosh, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301022200 · Cited by 121
Self-citationLee, J., Jung, H. S., Giang, P. M., Jin, X., Lee, S., Son, P. T., Lee, D., Hong, Y., Lee, K., & Lee, J. J. (2005) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.092486 · Cited by 121
“271 at A SPE T Journals on A ugust 17, 2017 jpet.aspetjournals.org nloaded from ylation by IKK of I B proteins at specific serine residues, which target these proteins for ubiquitin conjugation and degradation by the 26S proteasome (Ghosh and Karin, 2002).”
BackgroundHistone methylation modifiers in cellular signaling pathways
Alam, H., Gu, B., & Lee, M. G. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2023-y · Cited by 124
Canonical and non-canonical NF-κB signaling promotes breast cancer tumor-initiating cells
Kendellen, M. F., Bradford, J. W., Lawrence, C. L., Clark, K. S., & Baldwin, A. S. (2013) · Oncogene · doi:10.1038/onc.2013.64 · Cited by 120
“IKK α typically acts in non-canonical NF-κ B signaling (reviewed in (15, 16)), although it has recently been reported to promote canonical NF-κ B signaling in breast cancer cells of the HER2+ subtype (33).”
InfluentialNF-κB prevents β cell death and autoimmune diabetes in NOD mice
Kim, S., Millet, I., Kim, H. S., Kim, J., Han, M. S., Lee, M., Kim, K., Sherwin, R. S., Karin, M., & Lee, M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610690104 · Cited by 119
Self-citationMarcus, J. S., Karackattu, S. L., Fleegal, M. A., & Sumners, C. (2002) · Glia · doi:10.1002/glia.10168 · Cited by 120
Endosomal Nox2 Facilitates Redox-Dependent Induction of NF-κB by TNF-α
Li, Q., Spencer, N. Y., Oakley, F. D., Buettner, G. R., & Engelhardt, J. F. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2407 · Cited by 119
“NF-k B, a ubiquitous transcription factor, has been shown to mediate the expression of genes responsible for the activation of immune and inflammatory responses (17).”
Westergaard, M., Henningsen, J., Rasmussen, S., Kristiansen, K., Johansen, C., Svendsen, M. L., Jensen, U. B., Schrøder, H. D., Staels, B., Iversen, L., et al. (2003) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2003.12536.x · Cited by 119
Medeiros, R., Figueiredo, C. P., Pandolfo, P., Duarte, F. S., Prediger, R. D. S., Passos, G. F., & Calixto, J. B. (2010) · Behavioural Brain Research · doi:10.1016/j.bbr.2010.01.040 · Cited by 121
Direct Transcriptional Regulation of RelB by 1α,25-Dihydroxyvitamin D3 and Its Analogs
Dong, X., Craig, T. A., Xing, N., Bachman, L. A., Payá, C. V., Weih, F., McKEAN, D. J., Kumar, R., & Griffin, M. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308448200 · Cited by 120
Shishodia, S., & Aggarwal, B. B. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0206 · Cited by 120
Oxidized ATP (oATP) attenuates proinflammatory signaling via P2 receptor‐independent mechanisms
Beigi, R. D., Kertesy, S. B., Aquilina, G. R., & Dubyak, G. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705470 · Cited by 120
“…internalized oATP might target the IkB-kinase complex that facilitates the British Journal of Pharmacology vol 140 (3) dissociation of cytosolic p50/p65/IkB complexes, rapid degradation of IkB, and consequent nuclear accumulation of transcriptionally active NF-kB subunits (Ghosh & Karin, 2002).”
Metadata
- Authors
- Ghosh, S., & Karin, M.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of California San Diego (US)
- Corresponding author
- Ghosh, Sankar
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2002-04
- Volume
- 109
- Issue
- 2
- Pages
- S81-S96
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1976382352
- Cited by
- 3,638
- References
- 158
- Citations by year
- 2026: 29 · 2025: 65 · 2024: 66 · 2023: 49 · 2022: 66 · 2021: 94 · 2020: 100 · 2019: 84 · 2018: 103 · 2017: 111 · 2016: 122 · 2015: 141 · 2014: 134 · 2013: 144 · 2012: 189
- FWCI
- 19.54
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- NF-κB, IκB kinase complex, transcription factor regulation, transcriptional activity, IκB, signal transduction
- MeSH terms
- Animals, Cell Nucleus, Cytoplasm, Enzyme Activation, Gene Expression Regulation, Humans, Signal Transduction, NF-kappa B, Protein Serine-Threonine Kinases, Catalytic Domain, Active Transport, Cell Nucleus, I-kappa B Kinase
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review